A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters.

A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters.
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DOI:
10.1039/c3cc48239a
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发表时间:
2014-04-14
期刊:
Chemical communications (Cambridge, England)
影响因子:
--
通讯作者:
Cowan JA
Cowan JA
中科院分区:
其他
文献类型:
--
作者:
Qi W;Li J;Cowan JA

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谷胱甘肽络合的[2Fe-2S]簇能显著刺激溶液和蛋白脂体结合形式(KD~68μM)的ABCB7型转运蛋白的ATPase活性。该簇可能是这种转运蛋白的天然底物,它参与了胞内Fe-S簇蛋白的成熟。在活性转运蛋白的新结构模型上确定了可能的底物结合位点。
Glutathione-complexed [2Fe-2S] cluster is shown to significantly stimulate the ATPase activity of an ABCB7-type transporter in both solution and proteoliposome-bound forms (KD ~ 68 μM). The cluster is a likely natural substrate for this transporter, which has been implicated in cytosolic Fe-S cluster protein maturation. A possible substrate-binding site is identified on a new structural model for the active transporter.
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